Gilvo_00070 Gilvo_00070   Gilvo_00090 Gilvo_00090

Gilvo_00080 : CDS information

close this sectionLocation

Organism
StrainGö 3592
Entry nameGilvocarcin
Contig
Start / Stop / Direction11,512 / 10,016 / - [in whole cluster]
11,512 / 10,016 / - [in contig]
Locationcomplement(10016..11512) [in whole cluster]
complement(10016..11512) [in contig]
TypeCDS
Length1,497 bp (498 aa)
Click on the icon to see Genetic map.

close this sectionAnnotation

Category3.3 modification reduction
ProductFAD-dependent C-6 dehydrogenase
Product (GenBank)putative oxidoreductase
Gene
Gene (GenBank)gilR
EC number
Keyword
  • lactone formation
Note
Note (GenBank)
  • GilR
Reference
ACC
PmId
[12822997] The complete gene cluster of the antitumor agent gilvocarcin V and its implication for the biosynthesis of the gilvocarcins. (J Am Chem Soc. , 2003)
[19388008] GilR, an unusual lactone-forming enzyme involved in gilvocarcin biosynthesis. (Chembiochem. , 2009)
[21561854] The crystal structure and mechanism of an unusual oxidoreductase, GilR, involved in gilvocarcin V biosynthesis. (J Biol Chem. , 2011)
[22800463] Roles of the synergistic reductive O-methyltransferase GilM and of O-methyltransferase GilMT in the gilvocarcin biosynthetic pathway. (J Am Chem Soc. , 2012)
comment
[PMID: 12822997](2003)
gilvocarcin(gil) gene cluster同定のためにクローニングされたcos-G9B3をS.lividans TK24に導入すると、wildレベルのgilvocarcins V and M産生あり。よってgilvocarcin生合成のための完全なclusterが含まれている。

cos-G9B3をサブクローニングしてシークエンス。32.9kbpに26ORFsあり。
supporting info. Table 1
GilR(498aa): Oxidoreductase

配列解析のみ

---
[PMID: 19388008](2009)
oxidoreductase GilRを精製し特徴づけ。
GilRはFADを使用してpregilvocarcin V→gilvocarcin V(GV)へのdehydrogenationを触媒してlactoneを形成することを実証。
これはGV生合成経路の最終ステップに当たる。

---
[PMID: 21561854](2011)
GilRとその基質pregilvocarcin Vの複合体を結晶構造解析。
GilRはcofactor FADで繋がれたdimerを形成。
mutagenesisと機能測定から触媒作用メカニズムを提唱。

---
[PMID: 22800463](2012)
GilMT and GilMの調査。
recombinant enzymesを使った合成中間体とのin vitro実験。

GilRはGilMが反応に利用するFADH2を供給し、GilMの反応によりFADはリサイクルされると提唱している。
defuco-gilvocarcin Mの産生量が産物5 + GilMより、産物5 + GilM + GilRで10倍増えることから、GilMはGilRと相乗的に働くことが確認されたと述べている。

close this sectionSequence

selected fasta
>FAD-dependent C-6 dehydrogenase [putative oxidoreductase]
MTASVPPFTVGREDPRYIELSHSDNHRFVVEPEEFFLPATPDDVVASLQKAVTEGRGVAC
RSGGHCGQDFVGTPRRDLVLDLHNLHAIGPAADGAGVRVGSGATVDQVQKALFRRWNAAL
PLGACSAVGMGGLVAGGGYGPLSRQLGLVVDHLHAVEVAVVDESRTVRLVTARADDTGDL
GELFWAHTGGGGGNFGVVTAYEFRSPEHLATEPVGLPRAAGRLHVQKVVFPWAMIDETSF
VTVMRRFFEWHERHSEPGSPESSLFATFFVNHVSSGVLQLMVQQDADVDPEGEILARFVA
SLTEGTGVVGIPRGGVMSWLTGTRYMSQADCGDVMGARSASKSAYHRAAPTDEQLSVLHR
HLHADHPGQASYVMFNSYGGEINRRGPSDAAVPQRDSVVKSSWFSAWQDAELDELHLGWL
RGLYEEFFAGTGGVPVTGGRTDGCYINYPDADLLDPARNRSGEPWHHLYYKDNYARLRSA
KRAWDPLNTFHHSMSIGL
selected fasta
>FAD-dependent C-6 dehydrogenase [putative oxidoreductase]
GTGACCGCTTCCGTACCGCCGTTCACGGTGGGCCGCGAGGACCCGCGGTACATCGAACTG
TCGCACTCGGACAACCACCGGTTCGTCGTCGAGCCCGAGGAGTTCTTCCTCCCCGCCACG
CCGGACGACGTCGTCGCCTCCCTGCAGAAGGCCGTCACGGAAGGGCGGGGGGTCGCCTGC
CGGTCCGGCGGTCACTGCGGCCAGGACTTCGTCGGCACGCCGCGCCGGGACCTCGTCCTG
GACCTGCACAACCTCCATGCCATCGGCCCGGCCGCGGACGGCGCCGGGGTGCGCGTCGGT
TCCGGTGCGACGGTCGACCAGGTCCAGAAGGCCCTGTTCCGCCGGTGGAACGCGGCCCTG
CCGCTCGGGGCCTGCTCCGCGGTCGGCATGGGCGGCCTGGTCGCCGGAGGTGGTTACGGG
CCGCTGTCGCGCCAGCTGGGGCTGGTGGTCGACCACCTGCACGCGGTGGAGGTCGCCGTC
GTCGACGAGTCCCGCACCGTTCGCCTCGTGACGGCGAGGGCCGACGACACCGGCGATCTC
GGTGAGCTCTTCTGGGCACACACCGGCGGTGGCGGCGGCAACTTCGGCGTGGTCACGGCG
TACGAGTTCCGCAGCCCGGAGCACCTCGCCACGGAACCCGTCGGCCTGCCCCGCGCCGCC
GGCCGACTGCACGTCCAGAAGGTGGTGTTCCCCTGGGCCATGATCGACGAGACGTCCTTC
GTCACTGTGATGAGACGTTTCTTCGAGTGGCATGAACGCCACTCCGAGCCGGGGTCGCCG
GAGTCCTCGCTGTTCGCCACCTTCTTCGTGAACCACGTCAGCTCGGGCGTCCTGCAGCTG
ATGGTCCAGCAGGACGCCGACGTGGACCCCGAGGGCGAGATCCTCGCGCGGTTCGTCGCG
TCCCTGACCGAGGGCACCGGCGTGGTGGGCATCCCCCGAGGGGGTGTCATGAGCTGGCTC
ACCGGAACCCGCTACATGAGTCAGGCCGACTGCGGTGACGTCATGGGCGCCCGCTCCGCC
TCCAAGTCCGCCTACCACCGCGCGGCACCCACCGACGAGCAGCTCTCGGTGCTCCACCGG
CACCTGCACGCCGACCACCCCGGCCAGGCCTCGTACGTCATGTTCAACAGCTACGGGGGA
GAGATCAACCGGCGGGGGCCGTCGGACGCCGCCGTCCCCCAGCGGGACTCCGTCGTGAAG
TCGTCCTGGTTCTCGGCCTGGCAGGACGCGGAGCTGGACGAGCTGCACCTCGGCTGGCTG
CGCGGGCTCTACGAGGAGTTCTTCGCCGGCACGGGAGGGGTGCCCGTCACCGGCGGCCGC
ACGGACGGCTGCTACATCAACTACCCCGACGCGGATCTCCTGGACCCGGCCCGCAACCGC
TCCGGGGAGCCCTGGCACCACCTGTACTACAAGGACAACTACGCCCGTCTGCGGTCGGCG
AAGCGCGCGTGGGACCCCTTGAACACCTTCCATCACAGCATGTCCATAGGACTCTGA

close this sectionFeature

BLASTP
Database:UniProtKB:2011_09 		show BLAST table
InterPro
Database:interpro:38.0
IPR006093 Oxygen oxidoreductase covalent FAD-binding site (Binding_site)
[32-65] PS00862
PS00862   OX2_COVAL_FAD
IPR006094 FAD linked oxidase, N-terminal (Domain)
[34-160] 2.80000000000001e-16 PF01565
PF01565   FAD_binding_4
IPR012951 Berberine/berberine-like (Domain)
[444-497] 1.3e-17 PF08031
PF08031   BBE
IPR016166 FAD-binding, type 2 (Domain)
[3-208] 8.30001403791589e-30 SSF56176
SSF56176   FAD-binding_2
[28-208] PS51387
PS51387   FAD_PCMH
IPR016168 FAD-linked oxidase, FAD-binding, subdomain 2 (Domain)
[97-204] 1e-05 G3DSA:3.30.465.20
G3DSA:3.30.465.20   FAD-linked_oxidase_FAD-bd_sub2
SignalP No significant hit
TMHMM No significant hit
Gilvo_00070 Gilvo_00070   Gilvo_00090 Gilvo_00090
Page top